Modeling of protein binary complexes using structural mass spectrometry data.

ABSTRACT: In this article, we describe a general approach to modeling the structure of binary protein complexes using structural mass spectrometry data combined with molecular docking. In the first step, hydroxyl radical mediated oxidative protein footprinting is used to identify residues that experience conformational reorganization due to binding or participate in the binding interface. In the second step, a three-dimensional atomic structure of the complex is derived by computational modeling. Homology modeling approaches are used to define the structures of the individual proteins if footprinting detects significant conformational reorganization as a function of complex formation. A three-dimensional model of the complex is constructed from these binary partners using the ClusPro program, which

SUBMITTER: Kamal JK 

PROVIDER: S-EPMC2144602 | biostudies-literature | 2008 Jan

REPOSITORIES: biostudies-literature